Alcohol oxidases are known to be produced by various microorganisms grown on methanol. These alcohol oxidases catalyze the reaction EQU RCH.sub.2 OH+O.sub.2 .fwdarw.RCHO+H.sub.2 O.sub.2
where R is hydrogen or a lower alkyl. Alcohol Oxidases can be used to remove oxygen from compatible solutions, as well as be used in the production of aldehydes (RCHO) and hydrogen peroxide (H.sub.2 O.sub.2). Where R represents the methyl group (CH.sub.3), alcohol oxidase is the enzyme that catalyzes the oxidation of methanol to formaldehyde and hydrogen peroxide.
The production of H.sub.2 O.sub.2 with alcohol oxidase is often desirable since such peroxide has application in bleaching components of detergents and the like. However, one problem in the production of alcohol oxidase from yeast extracts is that catalase levels remain significant in the extract. Catalase breaks down H.sub.2 O.sub.2 into water and oxygen, thus, seriously impairing potential uses of the alcohol oxidase extract.
Presently, when a production lot of alcohol oxidase is high in amount of catalase activity, i.e., has retained more than 10 percent of its original catalase activity, such a lot is unacceptable for commercial use and is discarded. The high level of catalase activity is represented by about 20 percent of the alcohol oxidase lots presently produced, hence, approximately one in every five is unacceptably high in catalase activity. Therefore, a method which would enable reduction of the catalase activity in the lots of alcohol oxidase originally high in catalase activity would thus permit the alcohol oxidase to be used rather than discarded and would therefore represent a significant contribution to the art.